Succinate-semialdehyde dehydrogenase

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Function

Succinate-semialdehyde dehydrogenase or α-ketoglutaric semialdehyde dehydrogenase or succinyl-CoA reductase (SSD) catalyzes the conversion of succinate semialdehyde, NAD+ and water to succinate, NADH and H+. SSD participates in glutamate and butyrate metabolism[1]. See also Aldehyde dehydrogenase.


Disease

SSD deficiency is a disorder of GABA metabolism with symptoms of seizures, delayed development and hypotonia[2].

Structural highlights

The active site of SSD contains the substrate succinate semialdehyde and the cofactor NADP[3]. Water molecules are shown as red spheres. Whole binding site.


Structure of succinate-semialdehyde dehydrogenase complex with NADPH and succinate semialdehyde (PDB code 3vz3).

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3D structures of succinate-semialdehyde dehydrogenase

Updated on 06-December-2023

References

  1. JAKOBY WB, SCOTT EM. Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase. J Biol Chem. 1959 Apr;234(4):937-40. PMID:13654295
  2. Gordon N. Succinic semialdehyde dehydrogenase deficiency (SSADH) (4-hydroxybutyric aciduria, gamma-hydroxybutyric aciduria). Eur J Paediatr Neurol. 2004;8(5):261-5. PMID:15341910 doi:http://dx.doi.org/10.1016/j.ejpn.2004.06.004
  3. Yuan Z, Yin B, Wei D, Yuan YR. Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase. J Struct Biol. 2013 May;182(2):125-35. doi: 10.1016/j.jsb.2013.03.001. Epub 2013 , Mar 13. PMID:23500184 doi:10.1016/j.jsb.2013.03.001

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